8UQX
Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 keV
Summary for 8UQX
| Entry DOI | 10.2210/pdb8uqx/pdb |
| Descriptor | Phosphotriesterase variant PTE-R18, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | apo-phosphotriesterase, 9.5 kev, hydrolase |
| Biological source | Brevundimonas diminuta |
| Total number of polymer chains | 2 |
| Total formula weight | 72724.08 |
| Authors | Breeze, C.W.,Frkic, R.L.,Campbell, E.C.,Jackson, C.J. (deposition date: 2023-10-25, release date: 2024-04-03, Last modification date: 2024-04-10) |
| Primary citation | Breeze, C.W.,Nakano, Y.,Campbell, E.C.,Frkic, R.L.,Lupton, D.W.,Jackson, C.J. Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase. Acta Crystallogr D Struct Biol, 80:289-298, 2024 Cited by PubMed Abstract: Lanthanide ions have ideal chemical properties for catalysis, such as hard Lewis acidity, fast ligand-exchange kinetics, high coordination-number preferences and low geometric requirements for coordination. As a result, many small-molecule lanthanide catalysts have been described in the literature. Yet, despite the ability of enzymes to catalyse highly stereoselective reactions under gentle conditions, very few lanthanoenzymes have been investigated. In this work, the mononuclear binding of europium(III) and gadolinium(III) to the active site of a mutant of the model enzyme phosphotriesterase are described using X-ray crystallography at 1.78 and 1.61 Å resolution, respectively. It is also shown that despite coordinating a single non-natural metal cation, the PTE-R18 mutant is still able to maintain esterase activity. PubMed: 38512071DOI: 10.1107/S2059798324002316 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.52 Å) |
Structure validation
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